2. Academic Validation
  3. Characterization of a potassium channel toxin from the Caribbean Sea anemone Stichodactyla helianthus

Characterization of a potassium channel toxin from the Caribbean Sea anemone Stichodactyla helianthus

  • Toxicon. 1995 May;33(5):603-13. doi: 10.1016/0041-0101(95)00013-c.
O Castañeda 1,  V Sotolongo,  A M Amor,  R Stöcklin,  A J Anderson,  A L Harvey,  A Engström,  C Wernstedt,  E Karlsson
Affiliations

Affiliation

  • 1 Facultad de Biología, Universidad de La Habana, Cuba.
PMID: 7660365 DOI: 10.1016/0041-0101(95)00013-c
Abstract

A peptide toxin, ShK, that blocks voltage-dependent potassium channels was isolated from the whole body extract of the Caribbean sea anemone Stichodactyla helianthus. It competes with dendrotoxin I and alpha-dendrotoxin for binding to synaptosomal membranes of rat brain, facilities acetylcholine release at an avian neuromuscular junction and suppresses K+ currents in rat dorsal root ganglion neurones in culture. Its amino acid sequence is R1SCIDTIPKS10RCTAFQCKHS20MKYRLSFCRK30TCGTC35. There is no homology with other K+ channel-blocking Peptides, except for BgK from the sea anemone Bunodosoma granulifera. ShK and BgK appear to be in a different structural class from other toxins affecting K+ channels.

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